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Volumn 10, Issue 18, 2010, Pages 3292-3320

A proteomics approach to study synergistic and antagonistic interactions of the fungal-bacterial consortium Fusarium oxysporum wild-type MSA 35

Author keywords

Biological control; Fungal proteomics; Fungal bacterial association; Microbiology

Indexed keywords

ANTIBIOTIC AGENT;

EID: 77956513486     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200900716     Document Type: Article
Times cited : (19)

References (84)
  • 1
    • 24944498493 scopus 로고    scopus 로고
    • Plant disease: A threat to global food security
    • DOI 10.1146/annurev.phyto.43.113004.133839
    • Strange, R. N., Scott, P. R., Plant disease: a threat to global food security. Annu. Rev. Phytopathol. 2005, 43, 83-116. (Pubitemid 41318866)
    • (2005) Annual Review of Phytopathology , vol.43 , pp. 83-116
    • Strange, R.N.1    Scott, P.R.2
  • 2
    • 0002704887 scopus 로고
    • Nelson, P. E., Toussoun, T. A., Cook, R. J. (Eds.), Pennsylvania State University Press, Pennsylvania
    • Armstrong, G. M., Armstrong, J. K., in: Nelson, P. E., Toussoun, T. A., Cook, R. J. (Eds.), Fusarium: Diseases, Biology, and Taxonomy, Pennsylvania State University Press, Pennsylvania 1981, pp. 391-399.
    • (1981) Fusarium: Diseases, Biology, and Taxonomy , pp. 391-399
    • Armstrong, G.M.1    Armstrong, J.K.2
  • 3
    • 70350134073 scopus 로고    scopus 로고
    • Microbiological control of soil-borne phytopathogenic fungi with special emphasis on wilt-inducing Fusarium oxysporum
    • Alabouvette, C., Olivain, C., Migheli, Q., Steinberg, C., Microbiological control of soil-borne phytopathogenic fungi with special emphasis on wilt-inducing Fusarium oxysporum. New Phytol. 2009, 184, 529-544.
    • (2009) New Phytol. , vol.184 , pp. 529-544
    • Alabouvette, C.1    Olivain, C.2    Migheli, Q.3    Steinberg, C.4
  • 5
    • 0344104337 scopus 로고
    • Fusarium antagonisti contro la tracheofusariosi del garofano
    • Aloi, C., Conti, A., Garibaldi, A., Fusarium antagonisti contro la tracheofusariosi del garofano. Colture Protette 1994, 23, 79-82.
    • (1994) Colture Protette , vol.23 , pp. 79-82
    • Aloi, C.1    Conti, A.2    Garibaldi, A.3
  • 8
    • 44849127289 scopus 로고    scopus 로고
    • Bacterial ectosymbionts and virulence silencing in a Fusarium oxysporum strain
    • Minerdi, D., Moretti, M., Gilardi, G., Gullino, M. L., Garibaldi, A., Bacterial ectosymbionts and virulence silencing in a Fusarium oxysporum strain. Environ. Microbiol. 2008, 10, 1725-1741.
    • (2008) Environ. Microbiol. , vol.10 , pp. 1725-1741
    • Minerdi, D.1    Moretti, M.2    Gilardi, G.3    Gullino, M.L.4    Garibaldi, A.5
  • 9
    • 63749088296 scopus 로고    scopus 로고
    • Volatile organic compounds: A potential direct long-distance mechanism for antagonistic action of Fusarium oxysporum strain MSA 35
    • Minerdi, D., Bossi, S., Gullino, M. L., Garibaldi, A., Volatile organic compounds: a potential direct long-distance mechanism for antagonistic action of Fusarium oxysporum strain MSA 35. Environ. Microbiol. 2009, 11, 844-854.
    • (2009) Environ. Microbiol. , vol.11 , pp. 844-854
    • Minerdi, D.1    Bossi, S.2    Gullino, M.L.3    Garibaldi, A.4
  • 10
    • 33847264492 scopus 로고    scopus 로고
    • The mixed xylem sap proteome of Fusarium oxysporum-infected tomato plants
    • Houterman, P. M., Speijer, D., Dekker, H. L., de Koster, C. G. et al., The mixed xylem sap proteome of Fusarium oxysporum-infected tomato plants. Mol. Plant Pathol. 2007, 8, 215-221.
    • (2007) Mol. Plant Pathol. , vol.8 , pp. 215-221
    • Houterman, P.M.1    Speijer, D.2    Dekker, H.L.3    De Koster, C.G.4
  • 11
    • 1542653554 scopus 로고    scopus 로고
    • Proteomics as a tool to monitor plant-microbe endosymbioses in the rhizosphere
    • Bestel-Corre, G., Dumas-Gaudot, E., Gianinazzi, S., Proteomics as a tool to monitor plant-microbe endosymbioses in the rhizosphere. Mycorrhiza 2004, 14, 1-10.
    • (2004) Mycorrhiza , vol.14 , pp. 1-10
    • Bestel-Corre, G.1    Dumas-Gaudot, E.2    Gianinazzi, S.3
  • 14
    • 21344433917 scopus 로고    scopus 로고
    • Proteomic response of the biological control fungus Trichoderma atroviride to growth on the cell walls of Rhizoctonia solani
    • Grinyer, J., Hunt, S., McKay, M., Herbert, B. R., Nevalainen, H., Proteomic response of the biological control fungus Trichoderma atroviride to growth on the cell walls of Rhizoctonia solani. Curr. Genet. 2005, 47, 381-388.
    • (2005) Curr. Genet. , vol.47 , pp. 381-388
    • Grinyer, J.1    Hunt, S.2    McKay, M.3    Herbert, B.R.4    Nevalainen, H.5
  • 15
    • 33750296845 scopus 로고    scopus 로고
    • Study of the three-way interaction between Trichoderma atroviride, plant and fungal pathogens by using a proteomic approach
    • Marra, R., Ambrosino, P., Carbone, V., Vinale, F. et al., Study of the three-way interaction between Trichoderma atroviride, plant and fungal pathogens by using a proteomic approach. Curr. Genet. 2006, 50, 307-321.
    • (2006) Curr. Genet. , vol.50 , pp. 307-321
    • Marra, R.1    Ambrosino, P.2    Carbone, V.3    Vinale, F.4
  • 16
    • 0000521840 scopus 로고
    • Development of a selective medium for quantitative isolation of Fusarium oxysporum from natural soils
    • Komada, H., Development of a selective medium for quantitative isolation of Fusarium oxysporum from natural soils. Rev. Plant Prot. Res. 1975, 8, 114-125.
    • (1975) Rev. Plant Prot. Res. , vol.8 , pp. 114-125
    • Komada, H.1
  • 17
    • 31344450199 scopus 로고    scopus 로고
    • Towards the proteome of Burkholderia cenocepacia H111: Setting up a 2-DE reference map
    • Riedel, K., Carranza, P., Gehrig, P., Potthast, F., Eberl, L., Towards the proteome of Burkholderia cenocepacia H111: setting up a 2-DE reference map. Proteomics 2006, 6, 207-216.
    • (2006) Proteomics , vol.6 , pp. 207-216
    • Riedel, K.1    Carranza, P.2    Gehrig, P.3    Potthast, F.4    Eberl, L.5
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., Cottrell, J. S., Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20, 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0034843744 scopus 로고    scopus 로고
    • Support vector machine approach for protein subcellular localization prediction
    • Hua, S. J., Sun, Z. R., A Support vector machine approach for protein subcellular localization prediction. Bioinformatics 2001, 17, 721-728. (Pubitemid 32851380)
    • (2001) Bioinformatics , vol.17 , Issue.8 , pp. 721-728
    • Hua, S.1    Sun, Z.2
  • 24
    • 0030624649 scopus 로고    scopus 로고
    • Are bacterial proteases important virulence factors?
    • Lantz, M. S., Are bacterial proteases important virulence factors? J. Periodontal Res. 1997, 32, 126-132.
    • (1997) J. Periodontal Res. , vol.32 , pp. 126-132
    • Lantz, M.S.1
  • 25
    • 18244374474 scopus 로고    scopus 로고
    • Up-regulation of Pr1, a subtilisin-like protease, during conidiation in the insect pathogen Metarhizium anisopliae
    • Small, C.-L. N., Bidochka, M. J., Up-regulation of Pr1, a subtilisin-like protease, during conidiation in the insect pathogen Metarhizium anisopliae. Mycol. Res. 2005, 109, 307-313.
    • (2005) Mycol. Res. , vol.109 , pp. 307-313
    • Small, C.-L.N.1    Bidochka, M.J.2
  • 26
    • 34548072220 scopus 로고    scopus 로고
    • Proteases from Bacillus: A new insight into the mechanism of action for rhizobacterial suppression of nematode populations
    • DOI 10.1111/j.1472-765X.2007.02184.x
    • Lian, L. H., Tian, B. Y., Xiong, R., Zhu, M. Z. et al., Proteases from Bacillus: a new insight into the mechanism of action for rhizobacterial suppression of nematode populations. Lett. Appl. Microbiol. 2007, 45, 262-269. (Pubitemid 47294729)
    • (2007) Letters in Applied Microbiology , vol.45 , Issue.3 , pp. 262-269
    • Lian, L.H.1    Tian, B.Y.2    Xiong, R.3    Zhu, M.Z.4    Xu, J.5    Zhang, K.Q.6
  • 27
    • 1042267972 scopus 로고    scopus 로고
    • Putative virulence factors are released in association with membrane vesicles from Burkholderia cepacia
    • Allan, N. D., Kooi, C., Sokol, P. A., Beveridge, T. J., Putative virulence factors are released in association with membrane vesicles from Burkholderia cepacia. Can. J. Microbiol. 2003, 49, 613-624.
    • (2003) Can. J. Microbiol. , vol.49 , pp. 613-624
    • Allan, N.D.1    Kooi, C.2    Sokol, P.A.3    Beveridge, T.J.4
  • 28
    • 25144442319 scopus 로고    scopus 로고
    • Extracellular protease of Pseudomonas fluorescens CHA0, a biocontrol factor with activity against the root-knot nematode Meloidogyne incognita
    • Siddiqui, I. A., Haas, D., Heeb, S., Extracellular protease of Pseudomonas fluorescens CHA0, a biocontrol factor with activity against the root-knot nematode Meloidogyne incognita. Appl. Environ. Microbiol. 2005, 71, 5646-5649.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 5646-5649
    • Siddiqui, I.A.1    Haas, D.2    Heeb, S.3
  • 29
    • 0035013630 scopus 로고    scopus 로고
    • Microbial interactions and biocontrol in the rhizosphere
    • Whipps, J. M., Microbial interactions and biocontrol in the rhizosphere. J. Exp. Bot. 2001, 52, 487-511.
    • (2001) J. Exp. Bot. , vol.52 , pp. 487-511
    • Whipps, J.M.1
  • 30
    • 3943062954 scopus 로고    scopus 로고
    • ATP-binding cassette transporters in bacteria
    • Davidson, A. L., Chen, J., ATP-binding cassette transporters in bacteria. Annu. Rev. Biochem. 2004, 73, 241-268.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 241-268
    • Davidson, A.L.1    Chen, J.2
  • 31
    • 34548035390 scopus 로고    scopus 로고
    • Identification and regulation of genes from a biocontrol strain of Fusarium oxysporum
    • Fravel, D. R., Moravec, B. C., Bailey, B. A., Identification and regulation of genes from a biocontrol strain of Fusarium oxysporum. J. Phytopathol. 2007, 155, 526-530.
    • (2007) J. Phytopathol. , vol.155 , pp. 526-530
    • Fravel, D.R.1    Moravec, B.C.2    Bailey, B.A.3
  • 32
    • 39749161043 scopus 로고    scopus 로고
    • Differential role of ferritins in iron metabolism and virulence of the plant-pathogenic bacterium Erwinia chrysanthemi 3937
    • Boughammoura, A., Matzanke, B. F., Bottger, L., Reverchon, S. et al., Differential role of ferritins in iron metabolism and virulence of the plant-pathogenic bacterium Erwinia chrysanthemi 3937. J. Bacteriol. 2008, 190, 1518-1530.
    • (2008) J. Bacteriol. , vol.190 , pp. 1518-1530
    • Boughammoura, A.1    Matzanke, B.F.2    Bottger, L.3    Reverchon, S.4
  • 33
    • 34248664407 scopus 로고    scopus 로고
    • Ferritins, bacterial virulence and plant defence
    • DOI 10.1007/s10534-006-9069-0, Biometals: function and transport in bacteria, fungi, and humans
    • Boughammoura, A., Franza, T., Dellagi, A., Roux, C. et al., Ferritins, bacterial virulence and plant defense. Biometals 2007, 20, 347-353. (Pubitemid 46776583)
    • (2007) BioMetals , vol.20 , Issue.3-4 , pp. 347-353
    • Boughammoura, A.1    Franza, T.2    Dellagi, A.3    Roux, C.4    Matzanke-Markstein, B.5    Expert, D.6
  • 34
    • 43449127513 scopus 로고    scopus 로고
    • Rho1 has distinct functions in morphogenesis, cell wall biosynthesis and virulence of Fusarium oxysporum
    • Martinez-Rocha, A. L., Roncero, M. I. G., López-Ramirez, A., Mariné, M. et al., Rho1 has distinct functions in morphogenesis, cell wall biosynthesis and virulence of Fusarium oxysporum. Cell. Microbiol. 2008, 10, 1339-1351.
    • (2008) Cell. Microbiol. , vol.10 , pp. 1339-1351
    • Martinez-Rocha, A.L.1    Roncero, M.I.G.2    López-Ramirez, A.3    Mariné, M.4
  • 35
    • 2942638202 scopus 로고    scopus 로고
    • Woronin body function in Magnaporthe grisea is essential for efficient pathogenesis and for survival during nitrogen starvation stress
    • Soundararajana, S., Jedd, G., Li, X., Ramos-Pamploñaa, M. et al., Woronin body function in Magnaporthe grisea is essential for efficient pathogenesis and for survival during nitrogen starvation stress. Plant Cell 2004, 16, 1564-1574.
    • (2004) Plant Cell , vol.16 , pp. 1564-1574
    • Soundararajana, S.1    Jedd, G.2    Li, X.3    Ramos-Pamploñaa, M.4
  • 36
    • 0037344723 scopus 로고    scopus 로고
    • The glyoxylate cycle is required for temporal regulation of virulence by the plant pathogenic fungus Magnaporthe grisea
    • Wang, Z.-Y., Thornton, C. R., Kershaw, M. J., Debao, L., Talbot, N. J., The glyoxylate cycle is required for temporal regulation of virulence by the plant pathogenic fungus Magnaporthe grisea. Mol. Microbiol. 2003, 47, 1601-1612.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1601-1612
    • Wang, Z.-Y.1    Thornton, C.R.2    Kershaw, M.J.3    Debao, L.4    Talbot, N.J.5
  • 37
    • 33750981838 scopus 로고    scopus 로고
    • NPS6, encoding a Nonribosomal Peptide Synthetase involved in siderophore-mediated iron metabolism, is a conserved virulence determinant of plant pathogenic ascomycetes
    • Oide, S., Moeder, W., Krasnoff, S., Gibson, D. et al., NPS6, encoding a Nonribosomal Peptide Synthetase involved in siderophore-mediated iron metabolism, is a conserved virulence determinant of plant pathogenic ascomycetes. Plant Cell 2006, 18, 2836-2853.
    • (2006) Plant Cell , vol.18 , pp. 2836-2853
    • Oide, S.1    Moeder, W.2    Krasnoff, S.3    Gibson, D.4
  • 39
    • 33646847604 scopus 로고    scopus 로고
    • Within-species Flagellin polymorphism in Xanthomonas campestris pv campestris and its impact on elicitation of Arabidopsis FLAGELLIN SENSING2-dependent defenses
    • Sun, W., Dunning, F. M., Pfund, C., Weingarten, R., Bent, A. F., Within-species Flagellin polymorphism in Xanthomonas campestris pv campestris and its impact on elicitation of Arabidopsis FLAGELLIN SENSING2-dependent defenses. Plant Cell 2006, 18, 764-779.
    • (2006) Plant Cell , vol.18 , pp. 764-779
    • Sun, W.1    Dunning, F.M.2    Pfund, C.3    Weingarten, R.4    Bent, A.F.5
  • 40
    • 0029913592 scopus 로고    scopus 로고
    • Flagellin A is essential for the virulence of Vibrio anguillarum
    • Milton, D. L., O'Toole, R., Horstedt, P., Wolf-Watz, H., Flagellin A is essential for the virulence of Vibrio anguillarum. J. Bacteriol. 1996, 178, 1310-1319.
    • (1996) J. Bacteriol. , vol.178 , pp. 1310-1319
    • Milton, D.L.1    O'Toole, R.2    Horstedt, P.3    Wolf-Watz, H.4
  • 41
    • 0033796984 scopus 로고    scopus 로고
    • High-affinity interaction between Gram-negative flagellin and a cell surface polypeptide results in human monocyte activation
    • McDermott, P. F., Ciacci-Woolwine, F., Snipes, J. A., Mizel, S. B., High-affinity interaction between Gram-negative flagellin and a cell surface polypeptide results in human monocyte activation. Infect. Immun. 2000, 68, 5525-5529.
    • (2000) Infect. Immun. , vol.68 , pp. 5525-5529
    • McDermott, P.F.1    Ciacci-Woolwine, F.2    Snipes, J.A.3    Mizel, S.B.4
  • 42
    • 0025788466 scopus 로고
    • Outer membrane protein a (OmpA) contributes to serum resistance and pathogenicity of Escherichia coli K-1
    • Weiser, J. N., Gotschlich, E. C., Outer membrane protein A (OmpA) contributes to serum resistance and pathogenicity of Escherichia coli K-1. Infect. Immun. 1991, 59, 2252-2258.
    • (1991) Infect. Immun. , vol.59 , pp. 2252-2258
    • Weiser, J.N.1    Gotschlich, E.C.2
  • 43
    • 27144529152 scopus 로고    scopus 로고
    • Tol-Pal proteins are critical cell envelope components of Erwinia chrysanthemi affecting cell morphology and virulence
    • Dubuisson, J. F., Vianney, A., Hugouvieux-Cotte-Pattat, N., Lazzaroni, J. C., Tol-Pal proteins are critical cell envelope components of Erwinia chrysanthemi affecting cell morphology and virulence. Microbiology 2005, 151, 3337-3347.
    • (2005) Microbiology , vol.151 , pp. 3337-3347
    • Dubuisson, J.F.1    Vianney, A.2    Hugouvieux-Cotte-Pattat, N.3    Lazzaroni, J.C.4
  • 44
    • 0037372822 scopus 로고    scopus 로고
    • DsbA of Pseudomonas aeruginosa is essential for multiple virulence factors
    • DOI 10.1128/IAI.71.3.1590-1595.2003
    • Ha, U. H., Wang, Y., Jin, S., DsbA of Pseudomonas aeruginosa is essential for multiple virulence factors. Infect. Immun. 2003, 71, 1590-1595. (Pubitemid 36254353)
    • (2003) Infection and Immunity , vol.71 , Issue.3 , pp. 1590-1595
    • Ha, U.-H.1    Wang, Y.2    Jin, S.3
  • 45
    • 4544229875 scopus 로고    scopus 로고
    • Two periplasmic disulfide oxidoreductases, DsbA and SrgA, target outer membrane protein SpiA, a component of the Salmonella pathogenicity island 2 Type III secretion system
    • Miki, T., Okada, N., Danbara, H., Two periplasmic disulfide oxidoreductases, DsbA and SrgA, target outer membrane protein SpiA, a component of the Salmonella pathogenicity island 2 Type III secretion system. J. Biol. Chem. 2004, 279, 34631-34642.
    • (2004) J. Biol. Chem. , vol.279 , pp. 34631-34642
    • Miki, T.1    Okada, N.2    Danbara, H.3
  • 46
    • 31844440317 scopus 로고    scopus 로고
    • Identification of a virulence-associated determinant, dihydrolipoamide dehydrogenase (lpd), in Mycoplasma gallisepticum through in vivo screening of transposon mutants
    • Hudson, P., Gorton, T. S., Papazisi, L., Cecchini, K. et al., Identification of a virulence-associated determinant, dihydrolipoamide dehydrogenase (lpd), in Mycoplasma gallisepticum through in vivo screening of transposon mutants. Infect. Immun. 2006, 74, 931-939.
    • (2006) Infect. Immun. , vol.74 , pp. 931-939
    • Hudson, P.1    Gorton, T.S.2    Papazisi, L.3    Cecchini, K.4
  • 47
    • 0036145495 scopus 로고    scopus 로고
    • Crystal structure of oxidized flavodoxin, an essential protein in Helicobacter pylori
    • DOI 10.1110/ps.28602
    • Freigang, J., Diederichs, K., Schäfer, K. P., Welte, W., Paul, R., Crystal structure of oxidized flavodoxin, an essential protein in Helicobacter pylori. Protein Sci. 2002, 11, 253-261. (Pubitemid 34075788)
    • (2002) Protein Science , vol.11 , Issue.2 , pp. 253-261
    • Freigang, J.1    Diederichs, K.2    Schafer, K.P.3    Welte, W.4    Paul, R.5
  • 48
    • 0036195722 scopus 로고    scopus 로고
    • α-Crystallin-type heat shock proteins: Socializing minichaperones in the context of a multichaperone network
    • Narberhaus, F., α-Crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. Microbiol. Mol. Biol. Rev. 2002, 66, 64-93.
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 64-93
    • Narberhaus, F.1
  • 49
    • 0032215072 scopus 로고    scopus 로고
    • Stress tolerance and metabolic response to stress in Drosophila melanogaster
    • Clark, A. G., Fucito, C. D., Stress tolerance and metabolic response to stress in Drosophila melanogaster. Heredity 1998, 81, 514-527.
    • (1998) Heredity , vol.81 , pp. 514-527
    • Clark, A.G.1    Fucito, C.D.2
  • 50
    • 34249067364 scopus 로고    scopus 로고
    • The 6-phosphogluconate dehydrogenase genes are responsive to abiotic stresses in rice
    • DOI 10.1111/j.1744-7909.2007.00460.x
    • Hou, F.-Y., Huang, J., Yu, S.-L., Zhang, H.-S., The 6-phosphogluconate dehydrogenase genes are responsive to abiotic stresses in rice. J. Integr. Plant Biol. 2007, 49, 655-663. (Pubitemid 46784762)
    • (2007) Journal of Integrative Plant Biology , vol.49 , Issue.5 , pp. 655-663
    • Hou, F.-Y.1    Huang, J.2    Yu, S.-L.3    Zhang, H.-S.4
  • 51
    • 0042261992 scopus 로고    scopus 로고
    • Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae
    • Shenton, D., Grant, C. M., Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae. Biochem. J. 2003, 374, 513-519.
    • (2003) Biochem. J. , vol.374 , pp. 513-519
    • Shenton, D.1    Grant, C.M.2
  • 52
    • 27144500828 scopus 로고    scopus 로고
    • Effects of exogenous factors on enzymes of carbon metabolism in thermoacidophilic bacteria of the genus Sulfobacillus
    • Krasil'nikova, E. N., Tsaplina, I. A., Zakharchuk, L. M., Bogdanova, T. I., Effects of exogenous factors on enzymes of carbon metabolism in thermoacidophilic bacteria of the genus Sulfobacillus. Appl. Biochem. Microbiol. 2001, 37, 358-362.
    • (2001) Appl. Biochem. Microbiol. , vol.37 , pp. 358-362
    • Krasil'nikova, E.N.1    Tsaplina, I.A.2    Zakharchuk, L.M.3    Bogdanova, T.I.4
  • 53
    • 15544377794 scopus 로고    scopus 로고
    • Molecular and evolutionary basis of the cellular stress response
    • Kültz, D., Molecular and evolutionary basis of the cellular stress response. Annu. Rev. Physiol. 2005, 67, 225-257.
    • (2005) Annu. Rev. Physiol. , vol.67 , pp. 225-257
    • Kültz, D.1
  • 54
    • 33846690105 scopus 로고    scopus 로고
    • Trypanosoma cruzi strains, Tulahuen 2 and Y, besides the difference in resistance to oxidative stress, display differential glucose-6-phosphate and 6-phosphogluconate dehydrogenases activities
    • Mielniczki-Pereira, A. A., Chiavegatto, C. M., Lopez, J. A., Colli, W. et al., Trypanosoma cruzi strains, Tulahuen 2 and Y, besides the difference in resistance to oxidative stress, display differential glucose-6-phosphate and 6-phosphogluconate dehydrogenases activities. Acta Tropica 2007, 101, 54-60.
    • (2007) Acta Tropica , vol.101 , pp. 54-60
    • Mielniczki-Pereira, A.A.1    Chiavegatto, C.M.2    Lopez, J.A.3    Colli, W.4
  • 55
    • 38649102163 scopus 로고    scopus 로고
    • Cometabolic degradation of polychlorinated biphenyls (PCBs) by axenic cultures of Ralstonia sp. strain SA-5 and Pseudomonas sp. strain SA-6 obtained from Nigerian contaminated soils
    • Adebusoye, S. A., Ilori, M. O., Picardal, F. W., Amund, O. O., Cometabolic degradation of polychlorinated biphenyls (PCBs) by axenic cultures of Ralstonia sp. strain SA-5 and Pseudomonas sp. strain SA-6 obtained from Nigerian contaminated soils. World J. Microbiol. Biotechnol. 2008, 24, 61-68.
    • (2008) World J. Microbiol. Biotechnol. , vol.24 , pp. 61-68
    • Adebusoye, S.A.1    Ilori, M.O.2    Picardal, F.W.3    Amund, O.O.4
  • 56
    • 33748751884 scopus 로고    scopus 로고
    • Quantification of homogentisate-1,2-dioxygenase expression in the fungus Exophiala lecanii-corni
    • Gunsch, C. K., Kinney, K. A., Szaniszlo, P. J., Whitman, C. P., Quantification of homogentisate-1,2-dioxygenase expression in the fungus Exophiala lecanii-corni. J. Microbiol. Methods 2006, 67, 257-265.
    • (2006) J. Microbiol. Methods , vol.67 , pp. 257-265
    • Gunsch, C.K.1    Kinney, K.A.2    Szaniszlo, P.J.3    Whitman, C.P.4
  • 57
    • 27144480805 scopus 로고    scopus 로고
    • Metabolic regulation at the tricarboxylic acid and glyoxylate cycles of the lignin-degrading basidiomycete Phanerochaete chrysosporium against exogenous addition of vanillin
    • Shimizu, M., Yuda, N., Nakamura, T., Tanaka, H., Wariishi, H., Metabolic regulation at the tricarboxylic acid and glyoxylate cycles of the lignin-degrading basidiomycete Phanerochaete chrysosporium against exogenous addition of vanillin. Proteomics 2005, 5, 3919-3931.
    • (2005) Proteomics , vol.5 , pp. 3919-3931
    • Shimizu, M.1    Yuda, N.2    Nakamura, T.3    Tanaka, H.4    Wariishi, H.5
  • 58
    • 33750589315 scopus 로고    scopus 로고
    • Impact of melanin on microbial virulence and clinical resistance to antimicrobial compounds
    • DOI 10.1128/AAC.00545-06
    • Nosanchuk, J. D., Casadevall, A., Impact of melanin on microbial virulence and clinical resistance to antimicrobial compounds. Agents Chemother. 2006, 50, 3519-3528. (Pubitemid 44684860)
    • (2006) Antimicrobial Agents and Chemotherapy , vol.50 , Issue.11 , pp. 3519-3528
    • Nosanchuk, J.D.1    Casadevall, A.2
  • 59
    • 0037977925 scopus 로고    scopus 로고
    • Investigating the role of polyols in Cladosporium fulvum during growth under hyper-osmotic stress and in planta
    • Clark,A. J., Blissett,K. J., Oliver,R. P., Investigating the role of polyols in Cladosporium fulvum during growth under hyper-osmotic stress and in planta. Planta 2003, 216, 614-619.
    • (2003) Planta , vol.216 , pp. 614-619
    • Clark, A.J.1    Blissett, K.J.2    Oliver, R.P.3
  • 60
    • 16844384914 scopus 로고    scopus 로고
    • A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid a with 4-amino-4-deoxy-L-arabinose. Identification and function of UDP-4-deoxy-4-form
    • Breazeale, S. D., Ribeiro, A. A., McClerren, A. L., Raetzm, C. R., A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-amino-4-deoxy-L-arabinose. Identification and function of UDP-4-deoxy-4-form. J. Biol. Chem. 2005, 280, 14154-14167.
    • (2005) J. Biol. Chem. , vol.280 , pp. 14154-14167
    • Breazeale, S.D.1    Ribeiro, A.A.2    McClerren, A.L.3    Raetzm, C.R.4
  • 61
    • 17644410810 scopus 로고    scopus 로고
    • Transcriptional regulation of the 4-amino-4-deoxy-l-arabinose biosynthetic genes in Yersinia pestis
    • Winfield, M. D., Latifi, T., Groisman, E. A., Transcriptional regulation of the 4-amino-4-deoxy-l-arabinose biosynthetic genes in Yersinia pestis. J. Biol. Chem. 2005, 280, 14765-14772.
    • (2005) J. Biol. Chem. , vol.280 , pp. 14765-14772
    • Winfield, M.D.1    Latifi, T.2    Groisman, E.A.3
  • 62
    • 24344489015 scopus 로고    scopus 로고
    • Proteomic analysis reveals the participation of energy- And stress-related proteins in the response of Pseudomonas putida DOT-T1E to toluene
    • Segura, A., Godoy, P., van Dillewijn, P., Hurtado, A. et al., Proteomic analysis reveals the participation of energy- and stress-related proteins in the response of Pseudomonas putida DOT-T1E to toluene. J. Bacteriol. 2005, 187, 5937-5945.
    • (2005) J. Bacteriol. , vol.187 , pp. 5937-5945
    • Segura, A.1    Godoy, P.2    Van Dillewijn, P.3    Hurtado, A.4
  • 64
    • 11344275778 scopus 로고    scopus 로고
    • First proteomic analysis of Legionella pneumophila based on its developing genome sequence
    • Lebeau, I., Lammertyn, E., De Buck, E., Maes, L. et al., First proteomic analysis of Legionella pneumophila based on its developing genome sequence. Res. Microbiol. 2005, 156, 119-129.
    • (2005) Res. Microbiol. , vol.156 , pp. 119-129
    • Lebeau, I.1    Lammertyn, E.2    De Buck, E.3    Maes, L.4
  • 65
    • 33847106987 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis protein profile of the phytopathogenic fungus Botrytis cinerea
    • Fernández-Acero, F. J., Jorge, I., Calvo, E., Vallejo, I. et al., Two-dimensional electrophoresis protein profile of the phytopathogenic fungus Botrytis cinerea. Proteomics 2006, 6, S88-S96.
    • (2006) Proteomics , vol.6
    • Fernández-Acero, F.J.1    Jorge, I.2    Calvo, E.3    Vallejo, I.4
  • 67
    • 0032126279 scopus 로고    scopus 로고
    • Alfalfa malate dehydrogenase (MDH): Molecular cloning and characterization of five different forms reveals a unique nodule-enhanced MDH
    • DOI 10.1046/j.1365-313X.1998.00192.x
    • Miller, S. S., Driscoll, B. T., Gregerson, R. G., Gantt, J. S., Vance, C. P., Alfalfa malate dehydrogenase (MDH): molecular cloning and characterization of five different forms reveals a unique nodule-enhanced MDH. Plant J. 1998, 15, 173-184. (Pubitemid 28371626)
    • (1998) Plant Journal , vol.15 , Issue.2 , pp. 173-184
    • Miller, S.S.1    Driscoll, B.T.2    Gregerson, R.G.3    Gantt, J.S.4    Vance, C.P.5
  • 68
    • 67349172847 scopus 로고    scopus 로고
    • Inter-kingdom encounters:recent advances in molecular bacterium-fungus interactions
    • Tarkka, M. T., Sarniguet, a., frey-Klett, P., Inter-kingdom encounters:recent advances in molecular bacterium-fungus interactions. Curr. Genet. 2009, 55, 233-243.
    • (2009) Curr. Genet. , vol.55 , pp. 233-243
    • Tarkka, M.T.1    Sarniguet, A.2    Frey-Klett, P.3
  • 69
    • 0033846005 scopus 로고    scopus 로고
    • Proteome analysis of differentially displayed proteins as a tool for the investigation of symbiosis
    • Natera, S. H. A., Guerreiro, N., Djordjevic, N. A., Proteome analysis of differentially displayed proteins as a tool for the investigation of symbiosis. Mol. Plant Microbe Interact. 2000, 13, 995-1009.
    • (2000) Mol. Plant Microbe Interact. , vol.13 , pp. 995-1009
    • Natera, S.H.A.1    Guerreiro, N.2    Djordjevic, N.A.3
  • 70
    • 0035101168 scopus 로고    scopus 로고
    • Proteome analysis of cultivar-specific interactions between Rhizobium legumino-sarum biovar trifolii and subterranean clover cultivar Woogenellup
    • Morris, A. C., Djordjevic, M. A., Proteome analysis of cultivar-specific interactions between Rhizobium legumino-sarum biovar trifolii and subterranean clover cultivar Woogenellup. Electrophoresis 2001, 22, 586-598.
    • (2001) Electrophoresis , vol.22 , pp. 586-598
    • Morris, A.C.1    Djordjevic, M.A.2
  • 71
    • 34047255890 scopus 로고    scopus 로고
    • Lectins: Carbohydrate-specific reagents and biological recognition molecules
    • Sharon, N., Lectins: carbohydrate-specific reagents and biological recognition molecules. J. Biol. Chem. 2007, 282, 2753-2764.
    • (2007) J. Biol. Chem. , vol.282 , pp. 2753-2764
    • Sharon, N.1
  • 72
    • 0033773038 scopus 로고    scopus 로고
    • Interactions between arbuscular mycorrhizal fungi and other microbial inoculants (Azospirillum, Pseudomonas, Trichoderma) and their effects on microbial population and enzyme activities in the rhizosphere of maize plants
    • Vázquez, M. M., César, S., Azcón, R., Barea, J. M., Interactions between arbuscular mycorrhizal fungi and other microbial inoculants (Azospirillum, Pseudomonas, Trichoderma) and their effects on microbial population and enzyme activities in the rhizosphere of maize plants. Appl. Soil Ecol. 2000, 15, 261-272.
    • (2000) Appl. Soil Ecol. , vol.15 , pp. 261-272
    • Vázquez, M.M.1    César, S.2    Azcón, R.3    Barea, J.M.4
  • 73
    • 0019349160 scopus 로고
    • Interaction of Bacteria and Fungi with lectins and lectin-like substances
    • Pistole, T. G., Interaction of Bacteria and Fungi with lectins and lectin-like substances. Annu. Rev. Microbiol. 1981, 35, 85-112.
    • (1981) Annu. Rev. Microbiol. , vol.35 , pp. 85-112
    • Pistole, T.G.1
  • 74
    • 0032773090 scopus 로고    scopus 로고
    • Transcription of a gene encoding a lectinlike glycoprotein is induced in root cells harboring arbuscular mycorrhizal fungi in Pisum sativum
    • Balestrini, R., Perotto, S., Gasverde, E., Dahiya, P. et al., Transcription of a gene encoding a lectinlike glycoprotein is induced in root cells harboring arbuscular mycorrhizal fungi in Pisum sativum. Mol. Plant Microbe Interact. 1999, 12, 785-791.
    • (1999) Mol. Plant Microbe Interact. , vol.12 , pp. 785-791
    • Balestrini, R.1    Perotto, S.2    Gasverde, E.3    Dahiya, P.4
  • 75
    • 0033916611 scopus 로고    scopus 로고
    • Genes expressed in Pseudomonas putida during colonization of a plant-pathogenic fungus
    • Lee, S.-W., Cooksey, D. A., Genes expressed in Pseudomonas putida during colonization of a plant-pathogenic fungus. Appl. Environ. Microbiol. 2000, 66, 2764-2772.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2764-2772
    • Lee, S.-W.1    Cooksey, D.A.2
  • 76
    • 18244362036 scopus 로고    scopus 로고
    • Imidazole antibiotics inhibit the nitric oxide dioxygenase function of microbial flavohemoglobin
    • Helmick, R. A., Fletcher, A. E., Gardner, A. M., Gessner, C. R. et al., Imidazole antibiotics inhibit the nitric oxide dioxygenase function of microbial flavohemoglobin. Antimicrob. Agents Chemother. 2005, 49, 1837-1843.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 1837-1843
    • Helmick, R.A.1    Fletcher, A.E.2    Gardner, A.M.3    Gessner, C.R.4
  • 77
    • 0031421691 scopus 로고    scopus 로고
    • The metabolism of 4-aminobutyrate (GABA) in fungi
    • Kumar, S., Punekar, N. S., The metabolism of 4-aminobutyrate (GABA) in fungi. Mycol. Res. 1997, 101, 403-409.
    • (1997) Mycol. Res. , vol.101 , pp. 403-409
    • Kumar, S.1    Punekar, N.S.2
  • 78
    • 0000307532 scopus 로고
    • Ethylene effects on in vitro and in vivo growth of certain postharvest fruit-infecting fungi
    • El-Kazzaz, M. K., Sommer, N. F., Kader, A. A., Ethylene effects on in vitro and in vivo growth of certain postharvest fruit-infecting fungi. Phytopathology 1983, 73, 998-1001.
    • (1983) Phytopathology , vol.73 , pp. 998-1001
    • El-Kazzaz, M.K.1    Sommer, N.F.2    Kader, A.A.3
  • 79
    • 0028052463 scopus 로고
    • Involvement of ethylene in spore germination and mycelial growth of Alternaria alternata
    • Kepczyńska, E., Involvement of ethylene in spore germination and mycelial growth of Alternaria alternata. Mycol. Res. 1994, 98, 118-120.
    • (1994) Mycol. Res. , vol.98 , pp. 118-120
    • Kepczyńska, E.1
  • 80
    • 77953324436 scopus 로고    scopus 로고
    • Ethylene production by Botrytis cinerea (causal organism of gray mold disease) and influence of the exogenously applied growth regulators and their inhibitor on disease development
    • Hardan, K., Al-Masri, M. I., Barakat, R., Ethylene production by Botrytis cinerea (causal organism of gray mold disease) and influence of the exogenously applied growth regulators and their inhibitor on disease development. Hebron Univ. Res. J. 2005, 2, 55-75.
    • (2005) Hebron Univ. Res. J. , vol.2 , pp. 55-75
    • Hardan, K.1    Al-Masri, M.I.2    Barakat, R.3
  • 81
    • 0036801379 scopus 로고    scopus 로고
    • New reactions in clavulanic acid biosynthesis
    • Townsend, C. A., New reactions in clavulanic acid biosynthesis. Curr. Opin. Chem. Biol. 2002, 6, 583-589.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 583-589
    • Townsend, C.A.1
  • 82
    • 0016152565 scopus 로고
    • Regulation of the pentose phosphate pathway in the fungus Aspergillus nidulans the Effect of Growth with nitrate
    • Hankinson, O., Cove, D. J., Regulation of the pentose phosphate pathway in the fungus Aspergillus nidulans The Effect of Growth with nitrate. J. Biol. Chem. 1974 249:2344-2353.
    • (1974) J. Biol. Chem. , vol.249 , pp. 2344-2353
    • Hankinson, O.1    Cove, D.J.2
  • 83
    • 26944498638 scopus 로고    scopus 로고
    • Cytidine deaminase activity in Penicillium politans NRC-510
    • Elshafei, A. M., Ali, N. H., Mohamed, L. A., Cytidine deaminase activity in Penicillium politans NRC-510. J. Basic Microbiol. 2005, 45, 335-343.
    • (2005) J. Basic Microbiol. , vol.45 , pp. 335-343
    • Elshafei, A.M.1    Ali, N.H.2    Mohamed, L.A.3
  • 84
    • 77149152780 scopus 로고    scopus 로고
    • Environmental proteomics: Analysis of structure and function of microbial communities
    • Schneider, T., Riedel, K., Environmental proteomics: analysis of structure and function of microbial communities. Proteomics 2010, 10, 785-798.
    • (2010) Proteomics , vol.10 , pp. 785-798
    • Schneider, T.1    Riedel, K.2


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